Product Details

Purity

>85% (SDS-PAGE)

Target Names

Uniprot No.

Q9IH63

Alternative Names

FFusion glycoprotein F0; Protein F) [Cleaved into: Fusion glycoprotein F2; Fusion glycoprotein F1]

Species

Nipah virus

Protein Length

Partial

Tag Info

Tag type will be determined during the manufacturing process.

The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Form

Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer before Lyophilization

Tris/PBS-based buffer, 6% Trehalose.

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet

Please contact us to get it.

Target Background

Function

Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with G at the virion surface. Upon G binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis.

Gene References into Functions

Using both coimmunoprecipitation and flow-cytometric strategies, we found a bidentate interaction between Nipah virus (NiV) G and F, where both the stalk and head regions of NiV G interact with F. This is a new structural-biological finding for the paramyxoviruses. Additionally, our studies disclosed regions of the NiV G and F glycoproteins dispensable for the G and F interactions. PMID: 27654290
Deletions of more than four residues in F protein did not affect F uptake or endosomal cleavage but downregulated the surface expression, likely by delaying the intracellular trafficking through endosomal-recycling compartments. PMID: 26059400
Data suggest that fusion of Nipah viruses with host cells is facilitated by two of viral membrane proteins, G and F proteins; G protein binds to human ephrins B2 and B3; this interaction triggers F protein to mediate virus-host fusion. PMID: 24615845
These findings are consistent with a general mechanism of paramyxovirus fusion activation in which the stalk domain of the receptor binding protein is responsible for F activation. PMID: 23903846
These findings suggest that the G-F interaction is not mediated entirely by the stalk domain of G. PMID: 23283956
Activation of the Nipah virus fusion protein is mediated by cathepsin B within the endosome. PMID: 22278224
The authors conclude that distribution of Nipah virus F and G glycoproteins is responsible for lateral virus spread in both, epithelial and endothelial cell monolayers. PMID: 21054904
galectin-1 reduces NiV-F mediated fusion of endothelial cells, and endogenous galectin-1 in endothelial cells is sufficient to inhibit syncytia formation PMID: 20657665
The results suggest that basolateral or bipolar F and G expression facilitates the spread of Nipah virus within epithelial cell monolayers, thereby contributing to efficient virus spread in mucosal surfaces in early and late phases of infection. PMID: 20484517
F endocytosis clearly depended on a membrane-proximal YXXPhi motif and was found to be of functional importance for the biological activity of the protein. PMID: 15731282
N-glycans on Nipah virus fusion protein play varied roles in the pathobiology of NiV entry but also shed light on the general mechanisms of paramyxovirus fusion with host cells. PMID: 16641279
Polybasic KKR motif in the cytoplasmic tail of Nipah virus fusion protein modulates membrane fusion by inside-out signaling. PMID: 17301148
A multibasic cleavage peptide in the Nipah virus F protein completely impairs proteolytic processing and the generation of biological activity. PMID: 19665506

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Subcellular Location

Virion membrane; Single-pass type I membrane protein. Host cell membrane; Single-pass membrane protein.

Protein Families

Paramyxoviruses fusion glycoprotein family

Database Links

KEGG: vg:920954

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Recombinant Nipah virus Fusion glycoprotein F0 (F), partial

Product Details

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Target Background

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